Evidence map›Paper›PMID 24302572›Full record

ArticleeLife2013

Mechanism of chiral proofreading during translation of the genetic code.

Sadeem Ahmad, Satya Brata Routh, Venu Kamarthapu, Jisha Chalissery, Sowndarya Muthukumar, Tanweer Hussain, Shobha P Kruparani, Mandar V Deshmukh, Rajan Sankaranarayanan

Abstract read
In one paragraph

Article in eLife, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed.

  1. Article
  2. Chirality Makes or Breaks Chemically Driven Self-Assembly.Angewandte Chemie (International ed. in English) · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Distinct localization of chiral proofreaders resolves organellar translation conflict in plants.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Chiral checkpoints during protein biosynthesis.The Journal of biological chemistry · 2019
    Review
  15. Article
  16. Article
  17. Fluorothreonyl-tRNA deacylase prevents mistranslation in the organofluorine producerProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Sadeem AhmadStructural Biology Laboratory, Centre for Cellular and Molecular Biology, Council for Scientific and Industrial Research, Hyderabad, India.
Satya Brata Routh
Venu Kamarthapu
Jisha Chalissery
Sowndarya Muthukumar
Tanweer Hussain
Shobha P Kruparani
Mandar V Deshmukh
Rajan Sankaranarayanan

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biological macromolecular world is homochiral and effective enforcement and perpetuation of this homochirality is essential for cell survival. In this study, we present the mechanistic basis of a configuration-specific enzyme that selectively removes D-amino acids erroneously coupled to tRNAs. The crystal structure of dimeric D-aminoacyl-tRNA deacylase (DTD) from Plasmodium falciparum in complex with a substrate-mimicking analog shows how it uses an invariant 'cross-subunit' Gly-cisPro dipeptide to capture the chiral centre of incoming D-aminoacyl-tRNA. While no protein residues are directly involved in catalysis, the unique side chain-independent mode of substrate recognition provides a clear explanation for DTD's ability to act on multiple D-amino acids. The strict chiral specificity elegantly explains how the enriched cellular pool of L-aminoacyl-tRNAs escapes this proofreading step. The study thus provides insights into a fundamental enantioselection process and elucidates a chiral enforcement mechanism with a crucial role in preventing D-amino acid infiltration during the evolution of translational apparatus. DOI: http://dx.doi.org/10.7554/eLife.01519.001.

Indexed as

Genetic CodeStereoisomerismAdenosineCatalytic DomainCrystallizationDimerizationMolecular StructureAdenosineenzyme mechanismhomochiralityproofreadingtranslation

Identifiers

PMID24302572
PMCPMC3845328

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.